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The mechanism of the modifying effect of ATP on Na(+)-K+ ATPaseстатья
Информация о цитировании статьи получена из
Scopus
Дата последнего поиска статьи во внешних источниках: 28 мая 2015 г.
- Авторы: Boldyrev A.A., Fedosova N.U., Lopina O.D.
- Журнал: Biomedical science
- Том: 2
- Номер: 5
- Год издания: 1991
- Издательство: Academy Of Sciences Of The Ussr, Turpin Transactions Limited And Pion Limited
- Местоположение издательства: London, England
- Первая страница: 450
- Последняя страница: 454
- Аннотация: On the basis of a review of the literature and a study of the molecular and kinetic properties of Na(+)-K+ ATPase, a model is proposed that explains the regulation of the activity of the enzyme by ATP in terms of an acceleration of the E2----E1 transition. It is presumed that the transition occurs via a short-lived oligomer whose formation is accelerated by ATP. In the context of this model, the non-Michaelis-Menton kinetics of the enzyme can be explained by interprotomer interactions. After solubilization of the enzyme with octaethylene glycol dodecyl ether, the hydrolysis of ATP follows ordinary Michaelis-Menton kinetics. The validity of the model is also supported by radiation-inactivation experiments with a nucleotide (GTP) which does not accelerate the E2----E1 transition, as well as by experiments with a low concentration of ATP. In both situations, the size of the molecular target corresponds to the monomeric form of the enzyme.
- Добавил в систему: Лопина Ольга Дмитриевна